ArticleThe Journal of cell biology1985
Identification and localization of immunoreactive forms of caldesmon in smooth and nonmuscle cells: a comparison with the distributions of tropomyosin and alpha-actinin.
Article in The Journal of cell biology, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 171 citations in OpenAlex.
- Extracellular Matrix in Regulation of Contractile System in Cardiomyocytes.International journal of molecular sciences · 2019Review
- The conformational state of actin filaments regulates branching by actin-related protein 2/3 (Arp2/3) complex.The Journal of biological chemistry · 2012Article
- Histochemical localization of caldesmon isoforms in colon adenocarcinoma and lymph node metastases.Virchows Archiv : an international journal of pathology · 2011Article
- Histochemical localization of caldesmon in the CNS and ganglia of the mouse.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011Article
- The actin-binding protein caldesmon is in spleen and lymph nodes predominately expressed by smooth-muscle cells, reticular cells, and follicular dendritic cells.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2010Article
- New insights into the regulation of the actin cytoskeleton by tropomyosin.International review of cell and molecular biology · 2010Review
- Differential effects of caldesmon on the intermediate conformational states of polymerizing actin.The Journal of biological chemistry · 2010Article
- Glucocorticoid receptor-mediated expression of caldesmon regulates cell migration via the reorganization of the actin cytoskeleton.The Journal of biological chemistry · 2008Article
- Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008Review
- Alpha-smooth muscle actin expression upregulates fibroblast contractile activity.Molecular biology of the cell · 2001Article
- Mutant Caldesmon lacking cdc2 phosphorylation sites delays M-phase entry and inhibits cytokinesis.Molecular biology of the cell · 2001Article
- Vertebrate tropomyosin: distribution, properties and function.Journal of muscle research and cell motility · 2001Review
- Caldesmon inhibits nonmuscle cell contractility and interferes with the formation of focal adhesions.Molecular biology of the cell · 1999Article
- Identification and localization of caldesmon in cardiac muscle.The Biochemical journal · 1998Article
- Interaction of caldesmon with endoplasmic reticulum membrane: effects on the mobility of phospholipids in the membrane and on the phosphatidylserine base-exchange reaction.The Biochemical journal · 1997Article
- Phosphatidylserine liposomes can be tethered by caldesmon to actin filaments.Biophysical journal · 1997Article
- Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle.Journal of muscle research and cell motility · 1996Article
- Flexation of caldesmon: effect of conformation on the properties of caldesmon.Journal of muscle research and cell motility · 1995Article
- A 32-nucleotide exon-splicing enhancer regulates usage of competing 5' splice sites in a differential internal exon.Molecular and cellular biology · 1995Article
- Embryonic chicken gizzard: expression of the smooth muscle regulatory proteins caldesmon and myosin light chain kinase.Cell and tissue research · 1995Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caldesmon is an F-actin cross-linking protein of chicken gizzard smooth muscle whose F-actin binding activity can be regulated in vitro by Ca2+-calmodulin (Sobue, K., Y. Muramoto, M. Fujita, and S. Kakiuchi, 1981, Proc. Natl. Acad. Sci. USA, 78:5652-5655). It is a rod-shaped, heat-stable, F-actin bundling protein and is the most abundant F-actin cross-linking protein of chicken gizzard smooth muscle presently known (Bretscher, A., 1984, J. Biol. Chem., 259:12873-12880). We report the use of polyclonal antibodies to caldesmon to investigate its distribution and localization in other cells. Using immune blotting procedures, we have detected immunoreactive, heat-stable forms of caldesmon in cultured cells having either approximately the same apparent polypeptide molecular weight as gizzard caldesmon (120,000-140,000) or a substantially lower molecular weight (71,000-77,000). Through use of affinity-purified antibodies in indirect immunofluorescence microscopy, we have localized the immunoreactive forms to the terminal web of the brush border of intestinal epithelial cells and to the stress fibers and ruffling membranes of cultured cells. At the light microscope level caldesmon is distributed in a periodic fashion along stress fibers that is coincident with the distribution of tropomyosin and complementary to the distribution of alpha-actinin.
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